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517 results on '"Finazzi‐Agrò, Alessandro"'

3. Pitfalls and solutions in assaying anandamide transport in cells[S]

Author

Oddi, Sergio, Fezza, Filomena, Catanzaro, Giuseppina, De Simone, Chiara, Pucci, Mariangela, Piomelli, Daniele, Finazzi-Agrò, Alessandro, and Maccarrone, Mauro

Subjects
Adsorption, Arachidonic Acids, Artifacts, Biological Transport, Cell Line, Tumor, Cell Proliferation, Endocannabinoids, Glass, Humans, Hydrophobic and Hydrophilic Interactions, Plastics, Polyunsaturated Alkamides, Silicates, Spectrometry, Fluorescence, Surface Properties, endocannabinoids, lipid efflux, glass coverslips, plasticware, biotinylated derivative of anandamide, confocal microscopy, Biochemistry and Cell Biology, Medical Biochemistry and Metabolomics, Biochemistry & Molecular Biology
Abstract

Nonspecific binding of anandamide to plastic exhibits many features that could be mistaken as biological processes, thereby representing an important source of conflicting data on the uptake and release of this lipophilic substance. Herein, we propose an improved method to assay anandamide transport, by using glass slides (i.e., coverslips) as physical support to grow cells. Although the results obtained using plastic do not differ significantly from those obtained using glass, the new procedure has the advantage of being faster, simpler, and more accurate. In fact, the lack of aspecific adsorption of anandamide to the glass surface yields a lower background and a higher precision and accuracy in determining transport kinetics, especially for the export process. Remarkably, the kinetic parameters of anandamide uptake obtained with the old and the new procedures may be similar or different depending on the cell type, thus demonstrating the complexity of the interference of plastic on the transport process. In addition, the novel procedure is particularly suitable for visualization and measurement of anandamide transport in intact cells by using a biotinylated derivative in confocal fluorescence microscopy.

Published
2010

4. Anandamide uptake by synaptosomes from human, mouse and rat brain: inhibition by glutamine and glutamate.

Author

Battista, Natalia, Bari, Monica, Finazzi-Agrò, Alessandro, and Maccarrone, Mauro

Subjects
Other Information and Computing Sciences, Medical Biochemistry and Metabolomics, Nutrition and Dietetics, Nutrition & Dietetics
Abstract

Anandamide (N-arachidonoylethanolamine, AEA) belongs to an emerging class of endogenous lipids, called "endocannabinoids". A specific AEA membrane transporter (AMT) allows the import of this lipid and its degradation by the intracellular enzyme AEA hydrolase. Here, we show that synaptosomes from human, mouse and rat brain might be an ideal ex vivo system for the study of: i) the accumulation of AEA in brain, and ii) the pharmacological properties of AMT inhibitors. Using this ex vivo system, we demonstrate for the first time that glutamine and glutamate act as non-competitive inhibitors of AEA uptake by human, mouse and rat brain AMT.

Published
2002

6. Molten globule monomers in human superoxide dismutase

Author

Silva, Norberto, Gratton, Enrico, Mei, Giampiero, Rosato, Nicola, Rusch, Ruth, and Finazzi-Agrò, Alessandro

Subjects
Biochemistry and Cell Biology, Physical Sciences, Biological Sciences, Circular Dichroism, Fluorescence Polarization, Guanidine, Guanidines, Humans, Kinetics, Protein Conformation, Protein Denaturation, Superoxide Dismutase, Temperature, HUMAN SUPEROXIDE DISMUTASE, TIME-RESOLVED FLUORESCENCE, GLOBAL ANALYSIS, CONFORMATIONAL SUBSTATES, MOLTEN GLOBULE STATE, Chemical Sciences, Biophysics, Biological sciences, Chemical sciences, Physical sciences
Abstract

The time-resolved fluorescence decay and anisotropy of Cu/Zn human superoxide dismutase (HSOD) were studied as a function of temperature and denaturant concentration. In addition, circular dichroism (CD) measurements were performed on HSOD as a function of denaturant concentration in the amide and aromatic regions. The time-resolved fluorescence decay results reveal the existence of structural microheterogeneity in HSOD. Furthermore, CD measurements and a global analysis decomposition of the time-resolved fluorescence decay over denaturant concentration shows the presence of an intermediate in the unfolding of HSOD by guanidinium hydrochloride. Considering our previous measurements of partially denatured HSOD as a function of protein concentration (Mei et al., Biochemistry 31 (1992) 7224-7230), our results strongly suggest that the unfolding intermediate is a monomer that displays a molten globule state.

Published
1993

7. Dynamic fluorescence in copper proteins Selected examples

Author

Rosato, Nicola, Gratton, Enrico, Mei, Giampiero, Savini, Isabella, and Finazzi Agrò, Alessandro

Subjects
Biochemistry and Cell Biology, Biological Sciences, Azurin, Bacterial Proteins, Copper, Guanidine, Guanidines, Humans, Metalloproteins, Spectrometry, Fluorescence, Superoxide Dismutase, Temperature, Tryptophan, Biochemistry & Molecular Biology, Biochemistry and cell biology
Abstract

The fluorescence properties of three copper proteins, namely human superoxide dismutase, Pseudomonas aeruginosa azurin and Thiobacillus versutus amicyanin have been studied. All these proteins show a non-exponential decay of fluorescence, though the tryptophanyl residues responsible for the emission are very differently located in the three proteins. All the three decays can be fitted by at least two lifetimes or better with one or two lorentzian-shaped, continuous distributions of lifetime. In each case the removal of copper affects the quantum yield of fluorescence without affecting the shape of the emission.

Published
1990

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